CLTC

For other uses, see Christian Leaders' Training College.

CLTC
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2XZG, 4G55
Identifiers
Aliases	CLTC, CHC, CHC17, CLH-17, CLTCL2, Hc, clathrin heavy chain, MRD56
External IDs	OMIM: 118955 MGI: 2388633 HomoloGene: 3572 GeneCards: CLTC
Gene location (Human) Chr. Chromosome 17 (human) Band 17q23.1 Start 59,619,689 bp End 59,696,956 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11|11 C Start 86,585,177 bp End 86,648,391 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pons Brodmann area 46 middle temporal gyrus orbitofrontal cortex postcentral gyrus corpus epididymis trabecular bone visceral pleura caput epididymis bronchial epithelial cell Top expressed in habenula pontine nuclei medial geniculate nucleus medial dorsal nucleus medial vestibular nucleus dorsomedial hypothalamic nucleus lateral geniculate nucleus ventral tegmental area dorsal tegmental nucleus cerebellar vermis More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding double-stranded RNA binding protein kinase binding structural molecule activity RNA binding clathrin light chain binding disordered domain specific binding low-density lipoprotein particle receptor binding ubiquitin-specific protease binding Cellular component extracellular vesicle cytosol clathrin-coated endocytic vesicle membrane clathrin coat of coated pit trans-Golgi network membrane clathrin coat of trans-Golgi network vesicle focal adhesion melanosome plasma membrane endolysosome membrane clathrin-coated pit extracellular exosome cytoplasmic vesicle membrane cytoplasmic vesicle clathrin-coated vesicle extracellular matrix membrane mitotic spindle microtubule cytoplasm lysosome endosome spindle cytoskeleton clathrin coat clathrin complex protein-containing complex intracellular membrane-bounded organelle clathrin-coated endocytic vesicle mitotic spindle intracellular anatomical structure Biological process antigen processing and presentation of exogenous peptide antigen via MHC class II transferrin transport receptor internalization negative regulation of protein localization to plasma membrane retrograde transport, endosome to Golgi osteoblast differentiation vesicle-mediated transport negative regulation of hyaluronan biosynthetic process intracellular protein transport Wnt signaling pathway, planar cell polarity pathway regulation of mitotic spindle organization autophagy microtubule-based movement cell cycle cell division membrane organization mitotic cell cycle receptor-mediated endocytosis low-density lipoprotein particle receptor catabolic process low-density lipoprotein particle clearance clathrin coat assembly clathrin-dependent endocytosis amyloid-beta clearance by transcytosis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1213 67300 Ensembl ENSG00000141367 ENSMUSG00000047126 UniProt Q00610 Q68FD5 RefSeq (mRNA) NM_001288653 NM_004859 NM_001003908 NM_001356393 RefSeq (protein) NP_001275582 NP_004850 NP_001003908 NP_001343322 Location (UCSC) Chr 17: 59.62 – 59.7 Mb Chr 11: 86.59 – 86.65 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Clathrin heavy chain 1 is a protein that in humans is encoded by the CLTC gene.

Clathrin is a major protein component of the cytoplasmic face of intracellular organelles, called coated vesicles and coated pits. These specialized organelles are involved in the intracellular trafficking of receptors and endocytosis of a variety of macromolecules. The basic subunit of the clathrin coat is composed of three heavy chains and three light chains.

Interactions

CLTC has been shown to interact with PICALM and HGS.

See also

• Clathrin

References

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Further reading

• Murphy JE, Keen JH (1992). "Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia". J. Biol. Chem. 267 (15): 10850–5. doi:10.1016/S0021-9258(19)50096-5. PMID 1587861.
• Corvera S (1990). "Insulin stimulates the assembly of cytosolic clathrin onto adipocyte plasma membranes". J. Biol. Chem. 265 (5): 2413–6. doi:10.1016/S0021-9258(19)39811-4. PMID 2154445.
• Scarmato P, Kirchhausen T (1990). "Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3". J. Biol. Chem. 265 (7): 3661–8. doi:10.1016/S0021-9258(19)39644-9. PMID 2406259.
• Hanspal M, Luna E, Branton D (1984). "The association of clathrin fragments with coated vesicle membranes". J. Biol. Chem. 259 (17): 11075–82. doi:10.1016/S0021-9258(18)90624-1. PMID 6147350.
• Nomura N, Miyajima N, Sazuka T, et al. (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement)". DNA Res. 1 (1): 47–56. doi:10.1093/dnares/1.1.47. PMID 7584028.
• Fausser JL, Ungewickell E, Ruch JV, Lesot H (1994). "Interaction of vinculin with the clathrin heavy chain". J. Biochem. 114 (4): 498–503. doi:10.1093/oxfordjournals.jbchem.a124206. PMID 8276759.
• Kedra D, Peyrard M, Fransson I, et al. (1997). "Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11". Hum. Mol. Genet. 5 (5): 625–31. doi:10.1093/hmg/5.5.625. PMID 8733129.
• Goodman OB, Krupnick JG, Gurevich VV, et al. (1997). "Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain". J. Biol. Chem. 272 (23): 15017–22. doi:10.1074/jbc.272.23.15017. PMID 9169477.
• Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS (1997). "Identification and characterization of a nerve terminal-enriched amphiphysin isoform". J. Biol. Chem. 272 (26): 16700–6. doi:10.1074/jbc.272.26.16700. PMID 9195986.
• McMahon HT, Wigge P, Smith C (1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin". FEBS Lett. 413 (2): 319–22. doi:10.1016/S0014-5793(97)00928-9. PMID 9280305. S2CID 42520828.
• Foti M, Mangasarian A, Piguet V, et al. (1998). "Nef-mediated clathrin-coated pit formation". J. Cell Biol. 139 (1): 37–47. doi:10.1083/jcb.139.1.37. PMC 2139808. PMID 9314527.
• Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS (1998). "Association of the AP-3 adaptor complex with clathrin". Science. 280 (5362): 431–4. Bibcode:1998Sci...280..431D. doi:10.1126/science.280.5362.431. PMID 9545220.
• Ramjaun AR, McPherson PS (1998). "Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites". J. Neurochem. 70 (6): 2369–76. doi:10.1046/j.1471-4159.1998.70062369.x. PMID 9603201. S2CID 21910795.
• ter Haar E, Musacchio A, Harrison SC, Kirchhausen T (1998). "Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker". Cell. 95 (4): 563–73. doi:10.1016/S0092-8674(00)81623-2. PMC 4428171. PMID 9827808.
• Laporte SA, Oakley RH, Zhang J, et al. (1999). "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. Bibcode:1999PNAS...96.3712L. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
• Turner CE, Brown MC, Perrotta JA, et al. (1999). "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling". J. Cell Biol. 145 (4): 851–63. doi:10.1083/jcb.145.4.851. PMC 2133183. PMID 10330411.
• Hussain NK, Yamabhai M, Ramjaun AR, et al. (1999). "Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells". J. Biol. Chem. 274 (22): 15671–7. doi:10.1074/jbc.274.22.15671. PMID 10336464.
• Ybe JA, Brodsky FM, Hofmann K, et al. (1999). "Clathrin self-assembly is mediated by a tandemly repeated superhelix". Nature. 399 (6734): 371–5. Bibcode:1999Natur.399..371Y. doi:10.1038/20708. PMID 10360576. S2CID 4406014.

External links

• Human CLTC genome location and CLTC gene details page in the UCSC Genome Browser.